The preference for GT-rich DNA by the yeast Rad51 protein defines a set of universal pairing sequences

Robert B. Tracy, Jason K. Baumohl, Stephen C. Kowalczykowski

Research output: Contribution to journalArticlepeer-review

61 Scopus citations


The Rad51 protein of Saccharomyces cerevisiae is a eukaryotic homolog of the RecA protein, the prototypic DNA strand-exchange protein of Escherichia coli. RAD51 gene function is required for efficient genetic recombination and for DNA double-strand break repair. Recently, we demonstrated that RecA protein has a preferential affinity for GT-rich DNA sequences-several of which exhibit enhanced RecA protein-promoted homologous pairing activity. The fundamental similarity between the RecA and Rad51 proteins suggests that Rad51 might display an analogous bias. Using in vitro selection, here we show that the yeast Rad51 protein shares the same preference for GT-rich sequences as its prokaryotic counterpart. This bias is also manifest as an increased ability of Rad51 protein to promote the invasion of supercoiled DNA by homologous GT-rich single-stranded DNA, an activity not previously described for the eukaryotic pairing protein. We propose that the preferred utilization of GT-rich sequences is a conserved feature among all homologs of RecA protein, and that GT-rich regions are loci for increased genetic exchange in both prokaryotes and eukaryotes.

Original languageEnglish (US)
Pages (from-to)3423-3431
Number of pages9
JournalGenes and Development
Issue number24
StatePublished - Dec 15 1997


  • Genetic instability
  • Genetic recombination
  • Homologous pairing
  • In vitro selection
  • Rad51 protein

ASJC Scopus subject areas

  • Genetics
  • Developmental Biology


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